1ogt: Difference between revisions
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[[Image:1ogt.jpg|left|200px]]<br /><applet load="1ogt" size=" | [[Image:1ogt.jpg|left|200px]]<br /><applet load="1ogt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ogt, resolution 1.47Å" /> | caption="1ogt, resolution 1.47Å" /> | ||
'''CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)'''<br /> | '''CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OGT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain C'>AC1</scene>. Full crystallographic information is available from [http:// | 1OGT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: mhc (major histocompatibility complex)]] | [[Category: mhc (major histocompatibility complex)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:56 2008'' | ||
Revision as of 10:57, 3 February 2008
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CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)
OverviewOverview
The products of the human leukocyte antigen subtypes HLA-B*2705 and, HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide, binding groove but are differentially associated with the autoimmune, disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T, cell repertoires as exemplified by distinct T cell responses against the, self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show, that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705, molecules. In one binding mode, peptide pArg5 forms a salt bridge to, Asp116, connected with drastically different interactions between peptide, and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent, differences in pVIPR binding link the emergence of dissimilar T cell, repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried, Asp116/His116 polymorphism and provide novel insights into peptide, presentation by major histocompatibility antigens.
DiseaseDisease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
About this StructureAbout this Structure
1OGT is a Protein complex structure of sequences from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Dual, HLA-B27 subtype-dependent conformation of a self-peptide., Hulsmeyer M, Fiorillo MT, Bettosini F, Sorrentino R, Saenger W, Ziegler A, Uchanska-Ziegler B, J Exp Med. 2004 Jan 19;199(2):271-81. PMID:14734527
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